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Inspired by the complex influence of the globular crosslinking proteins onthe formation of biofilament bundles in living organisms, we study and analyzea theoretical model for the structure and thermodynamics of bundles of helicalfilaments assembled in the presence of crosslinking molecules. The helicalstructure of filaments, a universal feature of biopolymers such as filamentousactin, is shown to generically frustrate the geometry of crosslinking betweenthe "grooves" of two neighboring filaments. We develop a coarse-grained modelto investigate the interplay between the geometry of binding and mechanics ofboth linker and filament distortion, and we show that crosslinking in parallelbundles of helical filaments generates {\it intrinsic torques}, of the typethat tend to wind bundle superhelically about its central axis. Crosslinkingmediates a non-linear competition between the preference for bundle twist andthe size-dependent mechanical cost of filament bending, which in turn givesrise to feedback between the global twist of self-assembled bundles and theirlateral size. Finally, we demonstrate that above a critical density of boundcrosslinkers, twisted bundles form with a thermodynamically preferred radiusthat, in turn, increases with a further increase in crosslinking bonds. Weidentify the {\it stiffness} of crosslinking bonds as a key parameter governingthe sensitivity of bundle structure and assembly to the availability andaffinity of crosslinkers.

Theory of Crosslinked Bundles of Helical Filaments: Intrinsic Torques in Self-Limiting Biopolymer Assemblies